Conformational Changes at the Active Site of Pantetheine Hydrolase During Denaturation by Guanidine Hydrochloride View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1999-10

AUTHORS

Giuseppina Pitari, Angelo A. D'Archivio, Luana Di Leandro, Giovanni Antonini, Alberto Panatta, Enzo Tettamanti, Silvestro Duprè, Francesco Malatesta

ABSTRACT

Conformational changes at the active site of pantetheine hydrolase (EC3.5.1.-) during guanidine hydrochloride (GndHCl) denaturation were investigated by UV and circular dichroism spectroscopy and by electron spin resonance spectroscopy, following the spectral behaviour of the nitroxide radicals (N-(1-oxyl-2,2,5,5,-tetramethyl-3-pyrrolidinyl) iodacetamide) covalently linked to the two active site cysteine residues. At low denaturant concentrations (0.2 M) no conformational changes may be observed, whereas the catalytic activity, is strongly affected. The results indicate that the active site of pantetheine hydrolase is labile and unfolds under conditions in which no global tertiary structure modifications can be observed. More... »

PAGES

785-789

Identifiers

URI

http://scigraph.springernature.com/pub.10.1023/a:1020685619173

DOI

http://dx.doi.org/10.1023/a:1020685619173

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1031329289

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/10691189


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